SUMF1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SUMF1_HUMAN
• UniProt AC: Q8NBK3
• Protein Name: Formylglycine-generating enzyme {ECO:0000303|PubMed:12757705}
• Gene Name: SUMF1 {ECO:0000303|PubMed:12757706, ECO:0000312|HGNC:HGNC:20376}
• Organism: Homo sapiens (Human).
• Sequence Length: 374
• Subcellular Localization: Endoplasmic reticulum lumen .
• Protein Description: Oxidase that catalyzes the conversion of cysteine to 3-oxoalanine on target proteins, using molecular oxygen and an unidentified reducing agent. [PubMed: 12757706]
• Protein Sequence: MAAPALGLVCGRCPELGLVLLLLLLSLLCGAAGSQEAGTGAGAGSLAGSCGCGTPQRPGAHGSSAAAHRYSREANAPGPVPGERQLAHSKMVPIPAGVFTMGTDDPQIKQDGEAPARRVTIDAFYMDAYEVSNTEFEKFVNSTGYLTEAEKFGDSFVFEGMLSEQVKTNIQQAVAAAPWWLPVKGANWRHPEGPDSTILHRPDHPVLHVSWNDAVAYCTWAGKRLPTEAEWEYSCRGGLHNRLFPWGNKLQPKGQHYANIWQGEFPVTNTGEDGFQGTAPVDAFPPNGYGLYNIVGNAWEWTSDWWTVHHSVEETLNPKGPPSGKDRVKKGGSYMCHRSYCYRYRCAARSQNTPDSSASNLGFRCAADRLPTMD

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
100	Phosphorylation	PIPAGVFTMGTDDPQ EECCEEEECCCCCHH	16.57	-
103	Phosphorylation	AGVFTMGTDDPQIKQ CEEEECCCCCHHHCC	26.80	-
141	N-linked_Glycosylation	TEFEKFVNSTGYLTE HHHHHHHCCCCCCEE	36.67	15657036
141	N-linked_Glycosylation	TEFEKFVNSTGYLTE HHHHHHHCCCCCCEE	36.67	15657036
184	Acetylation	APWWLPVKGANWRHP CCCEEECCCCCCCCC	50.82	30592717
184	Ubiquitination	APWWLPVKGANWRHP CCCEEECCCCCCCCC	50.82	21963094
249	Ubiquitination	RLFPWGNKLQPKGQH CCCCCCCCCCCCCCC	44.56	-
344	Phosphorylation	HRSYCYRYRCAARSQ CHHHCHHHHHHHHCC	5.42	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of SUMF1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SUMF1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of SUMF1_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of SUMF1_HUMAN !!

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 272200: Multiple sulfatase deficiency (MSD)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-141, AND MASSSPECTROMETRY.
PubMed: 19159218

"Molecular basis for multiple sulfatase deficiency and mechanism forformylglycine generation of the human formylglycine-generatingenzyme.";
Dierks T., Dickmanns A., Preusser-Kunze A., Schmidt B., Mariappan M.,von Figura K., Ficner R., Rudolph M.G.;
Cell 121:541-552(2005).
Cited for: PARTIAL PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF73-374 IN COMPLEX WITH CALCIUM, GLYCOSYLATION AT ASN-141, MUTAGENESISOF SER-333; CYS-336; HIS-337; TYR-340 AND CYS-341, AND DISULFIDEBONDS.
PubMed: 15907468

"Molecular characterization of the human Calpha-formylglycine-generating enzyme.";
Preusser-Kunze A., Mariappan M., Schmidt B., Gande S.L., Mutenda K.,Wenzel D., von Figura K., Dierks T.;
J. Biol. Chem. 280:14900-14910(2005).
Cited for: PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, MASS SPECTROMETRY,CALCIUM-BINDING, GLYCOSYLATION AT ASN-141, SUBCELLULAR LOCATION, ANDDISULFIDE BONDS.
PubMed: 15657036